Extended Data Fig. 6: Conformational changes of the GDP/GTP-binding pocket of Gαi after β1-AR interaction. | Nature Structural & Molecular Biology

Extended Data Fig. 6: Conformational changes of the GDP/GTP-binding pocket of Gαi after β1-AR interaction.

From: Structural basis and mechanism of activation of two different families of G proteins by the same GPCR

Extended Data Fig. 6

(a) Comparison of the β1 strand, α1-helix and the β1-α1 loop of the Ras-like domains from β1-AR–Gi (in green) and from Gαi1Gβ1Gγ2 (PDB: 1GG2; in gray) when the Ras-like domains are superimposed. (b) Comparison of Switch II region from β1-AR–Gi and from Gαi1Gβ1Gγ2. (c) Comparison of Switch III region from β1-AR–Gi and from Gαi1Gβ1Gγ2. (d) Comparison of the regions from αG to α5-helix from β1-AR–Gi and from Gαi1Gβ1Gγ2. (E) Comparison of all GDP-interacting residues of the Ras-like domains from β1-AR–Gi and from Gαi1Gβ1Gγ2.

Back to article page